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Protein

Abnormal cell lineage protein 44

Gene

lin-44

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Ligand for members of the frizzled family of seven transmembrane receptors (By similarity). Affects male tail development, vulval precursor cell specification and egg laying. Involved in morphogenesis by influencing polarity of asymmetric cell divisions of the B, U, and F cells in the male, and the T cell in males and hermaphrodites. Controls spindle orientation in B-gamma cell division during male copulatory spicule development. Involved in specification of the P7.p lineage during vulval development. Has a role in providing polarity and default lin-17 localization in axon development and positioning of neuromuscular synapses in DA9 regions by negatively regulating synaptogenesis.By similarity17 Publications

GO - Molecular functioni

  • frizzled binding Source: WormBase

GO - Biological processi

  • cell fate specification involved in pattern specification Source: WormBase
  • establishment or maintenance of cell polarity Source: WormBase
  • interneuron migration Source: UniProtKB
  • motor neuron migration Source: UniProtKB
  • nematode male tail tip morphogenesis Source: WormBase
  • neuroblast migration Source: UniProtKB
  • neuron differentiation Source: GO_Central
  • neuron migration Source: UniProtKB
  • regulation of oviposition Source: WormBase
  • regulation of vulval development Source: WormBase
  • vulval development Source: WormBase
  • Wnt signaling pathway Source: WormBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Wnt signaling pathway

Enzyme and pathway databases

SignaLinkiQ27886.

Names & Taxonomyi

Protein namesi
Recommended name:
Abnormal cell lineage protein 44
Alternative name(s):
Wnt proteinImported
Gene namesi
Name:lin-44Imported
ORF Names:E01A2.3
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome I

Organism-specific databases

WormBaseiE01A2.3a; CE24870; WBGene00003029; lin-44.
E01A2.3b; CE36923; WBGene00003029; lin-44.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Disruption phenotypei

Cell fate decisions disrupted, protein localization altered and neuron translocation disrupted. Defective tail development in males. Defective in egg laying in hermaphrodites. Nuclear localization of wrm-1 and lit-1 appears disrupted. Similar to tau-induced unc phenotype. Deviations in vulval precursor cell fate are observed when knocked down in conjunction with cwn-1 and egl-20. Bivulval phenotype when accompanied by mom-2 and/or cwn-2 knockdowns. Increase in ectopic synaptic vesicle puncta.13 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence analysisAdd
BLAST
Chaini26 – 348323Abnormal cell lineage protein 44Sequence analysisPRO_0000400090Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi91 ↔ 102By similarity
Disulfide bondi141 ↔ 149By similarity
Disulfide bondi151 ↔ 165By similarity
Disulfide bondi213 ↔ 227By similarity
Disulfide bondi215 ↔ 222By similarity
Lipidationi219 – 2191O-palmitoleyl serine; by mom-1By similarity
Disulfide bondi282 ↔ 299By similarity
Glycosylationi286 – 2861N-linked (GlcNAc...)Sequence analysis
Disulfide bondi314 ↔ 338By similarity
Disulfide bondi314 ↔ 329By similarity
Disulfide bondi316 ↔ 326By similarity
Disulfide bondi321 ↔ 322By similarity

Post-translational modificationi

Palmitoleylation is required for efficient binding to frizzled receptors. Depalmitoleylation leads to Wnt signaling pathway inhibition.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein

Proteomic databases

PaxDbiQ27886.

Expressioni

Tissue specificityi

Expressed in the tail hypodermis.3 Publications

Developmental stagei

Expressed during embryogenesis and larval development.3 Publications

Interactioni

GO - Molecular functioni

  • frizzled binding Source: WormBase

Protein-protein interaction databases

BioGridi37465. 2 interactions.
STRINGi6239.E01A2.3a.

Structurei

3D structure databases

ProteinModelPortaliQ27886.
SMRiQ27886. Positions 71-339.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi294 – 32936Cys-richSequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the Wnt family.Sequence analysis

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG3913. Eukaryota.
ENOG410XQZ1. LUCA.
InParanoidiQ27886.
OMAiESAYLWA.
OrthoDBiEOG7SXW7G.
PhylomeDBiQ27886.

Family and domain databases

InterProiIPR005817. Wnt.
IPR018161. Wnt_CS.
[Graphical view]
PANTHERiPTHR12027. PTHR12027. 1 hit.
PfamiPF00110. wnt. 1 hit.
[Graphical view]
PRINTSiPR01349. WNTPROTEIN.
SMARTiSM00097. WNT1. 1 hit.
[Graphical view]
PROSITEiPS00246. WNT1. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform a2 Publications (identifier: Q27886-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MRAAPFDFFF QSTALSTFFI LCSLATNEIP TISGAPAGKI VQPPKPNILK
60 70 80 90 100
QGCPSDLLHS RALRSIQLAC RTHPATVISA FEGVQEGLQN CANRLRFQQW
110 120 130 140 150
DCSEAGNIMH DPPLLRQGFR ESSLIWALSS ASAAWGVATA CAQGWIDDCA
160 170 180 190 200
CNNQMGQNEY EFGGCTHGVQ HGITASRKLL TKVGAVNTLL RKVEKHNLKA
210 220 230 240 250
GRLAIKKTLI SSCKCHGVSG SCQQKTCWKR TATLEHITDY LVEKYARAKL
260 270 280 290 300
YTDDSVVKTT DLIYLEASPD VCKAKSVAGR VCAWRNETHT QGDCDRLCCG
310 320 330 340
NGFSIRHEVV RVKCDCEFVW CCNLVCKDCI QHRWISTCNG TPPKSLIF
Length:348
Mass (Da):38,381
Last modified:November 1, 1996 - v1
Checksum:i3DD9F50DF2C89C6D
GO
Isoform b1 Publication (identifier: Q27886-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     26-204: Missing.

Note: No experimental confirmation available.Curated
Show »
Length:169
Mass (Da):19,088
Checksum:iB72FBF18AFB19658
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei26 – 204179Missing in isoform b. 1 PublicationVSP_039999Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U22179 mRNA. Translation: AAA64846.1.
U22184 Genomic DNA. Translation: AAA64847.1.
FO081024 Genomic DNA. Translation: CCD68574.1.
FO081024 Genomic DNA. Translation: CCD68575.1.
PIRiA57234.
RefSeqiNP_001021081.1. NM_001025910.4. [Q27886-1]
UniGeneiCel.19749.

Genome annotation databases

EnsemblMetazoaiE01A2.3; E01A2.3; WBGene00003029. [Q27886-1]
GeneIDi171994.
KEGGicel:CELE_E01A2.3.
UCSCiE01A2.3b. c. elegans. [Q27886-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U22179 mRNA. Translation: AAA64846.1.
U22184 Genomic DNA. Translation: AAA64847.1.
FO081024 Genomic DNA. Translation: CCD68574.1.
FO081024 Genomic DNA. Translation: CCD68575.1.
PIRiA57234.
RefSeqiNP_001021081.1. NM_001025910.4. [Q27886-1]
UniGeneiCel.19749.

3D structure databases

ProteinModelPortaliQ27886.
SMRiQ27886. Positions 71-339.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi37465. 2 interactions.
STRINGi6239.E01A2.3a.

Proteomic databases

PaxDbiQ27886.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiE01A2.3; E01A2.3; WBGene00003029. [Q27886-1]
GeneIDi171994.
KEGGicel:CELE_E01A2.3.
UCSCiE01A2.3b. c. elegans. [Q27886-1]

Organism-specific databases

CTDi171994.
WormBaseiE01A2.3a; CE24870; WBGene00003029; lin-44.
E01A2.3b; CE36923; WBGene00003029; lin-44.

Phylogenomic databases

eggNOGiKOG3913. Eukaryota.
ENOG410XQZ1. LUCA.
InParanoidiQ27886.
OMAiESAYLWA.
OrthoDBiEOG7SXW7G.
PhylomeDBiQ27886.

Enzyme and pathway databases

SignaLinkiQ27886.

Miscellaneous databases

PROiQ27886.

Family and domain databases

InterProiIPR005817. Wnt.
IPR018161. Wnt_CS.
[Graphical view]
PANTHERiPTHR12027. PTHR12027. 1 hit.
PfamiPF00110. wnt. 1 hit.
[Graphical view]
PRINTSiPR01349. WNTPROTEIN.
SMARTiSM00097. WNT1. 1 hit.
[Graphical view]
PROSITEiPS00246. WNT1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Caenorhabditis elegans gene lin-44 controls the polarity of asymmetric cell divisions."
    Herman M.A., Horvitz H.R.
    Development 120:1035-1047(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
    Strain: Bristol N2Imported.
  2. "The C. elegans gene lin-44, which controls the polarity of certain asymmetric cell divisions, encodes a Wnt protein and acts cell nonautonomously."
    Herman M.A., Vassilieva L.L., Horvitz H.R., Shaw J.E., Herman R.K.
    Cell 83:101-110(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: Bristol N2Imported.
  3. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ALTERNATIVE SPLICING.
    Strain: Bristol N2.
  4. "Lineage-specific regulators couple cell lineage asymmetry to the transcription of the Caenorhabditis elegans POU gene unc-86 during neurogenesis."
    Baumeister R., Liu Y., Ruvkun G.
    Genes Dev. 10:1395-1410(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "C. elegans POP-1/TCF functions in a canonical Wnt pathway that controls cell migration and in a noncanonical Wnt pathway that controls cell polarity."
    Herman M.
    Development 128:581-590(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "C. elegans LIN-18 is a Ryk ortholog and functions in parallel to LIN-17/Frizzled in Wnt signaling."
    Inoue T., Oz H.S., Wiland D., Gharib S., Deshpande R., Hill R.J., Katz W.S., Sternberg P.W.
    Cell 118:795-806(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  7. "The C. elegans RUNX transcription factor RNT-1/MAB-2 is required for asymmetrical cell division of the T blast cell."
    Kagoshima H., Sawa H., Mitani S., Burglin T.R., Shigesada K., Kohara Y.
    Dev. Biol. 287:262-273(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  8. "Asymmetric cortical and nuclear localizations of WRM-1/beta-catenin during asymmetric cell division in C. elegans."
    Takeshita H., Sawa H.
    Genes Dev. 19:1743-1748(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  9. "A novel noncanonical Wnt pathway is involved in the regulation of the asymmetric B cell division in C. elegans."
    Wu M., Herman M.A.
    Dev. Biol. 293:316-329(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  10. "Multiple redundant Wnt signaling components function in two processes during C. elegans vulval development."
    Gleason J.E., Szyleyko E.A., Eisenmann D.M.
    Dev. Biol. 298:442-457(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  11. "Wnt signals and frizzled activity orient anterior-posterior axon outgrowth in C. elegans."
    Hilliard M.A., Bargmann C.I.
    Dev. Cell 10:379-390(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  12. "Wnt signals can function as positional cues in establishing cell polarity."
    Goldstein B., Takeshita H., Mizumoto K., Sawa H.
    Dev. Cell 10:391-396(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Molecular pathways that influence human tau-induced pathology in Caenorhabditis elegans."
    Kraemer B.C., Burgess J.K., Chen J.H., Thomas J.H., Schellenberg G.D.
    Hum. Mol. Genet. 15:1483-1496(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  14. "Wnt gradient formation requires retromer function in Wnt-producing cells."
    Coudreuse D.Y., Roel G., Betist M.C., Destree O., Korswagen H.C.
    Science 312:921-924(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  15. "Wnt signaling positions neuromuscular connectivity by inhibiting synapse formation in C. elegans."
    Klassen M.P., Shen K.
    Cell 130:704-716(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  16. "Cortical beta-catenin and APC regulate asymmetric nuclear beta-catenin localization during asymmetric cell division in C. elegans."
    Mizumoto K., Sawa H.
    Dev. Cell 12:287-299(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  17. "Wnt signal from multiple tissues and lin-3/EGF signal from the gonad maintain vulval precursor cell competence in Caenorhabditis elegans."
    Myers T.R., Greenwald I.
    Proc. Natl. Acad. Sci. U.S.A. 104:20368-20373(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  18. "Opposing Wnt pathways orient cell polarity during organogenesis."
    Green J.L., Inoue T., Sternberg P.W.
    Cell 134:646-656(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  19. "The roles of EGF and Wnt signaling during patterning of the C. elegans Bgamma/delta Equivalence Group."
    Seah A., Sternberg P.W.
    BMC Dev. Biol. 9:74-74(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiLIN44_CAEEL
AccessioniPrimary (citable) accession number: Q27886
Secondary accession number(s): Q6F3D0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 2, 2010
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.